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• W1974781808 abstract "Familial Mediterranean fever (FMF) is a recessively inherited autoinflammatory disorder with high carrier frequencies in the Middle East. Pyrin, the protein mutated in FMF, regulates caspase-1 activation and consequently IL-1β production through cognate interaction of its N-terminal PYRIN motif with the ASC adaptor protein. However, the preponderance of mutations reside in pyrin’s C-terminal B30.2 domain. Here we demonstrate direct interaction of this domain with caspase-1. In lysates from cells not expressing ASC, reciprocal GST pull-downs demonstrated the interaction of pyrin with the p20 and p10 catalytic subunits of caspase-1. Coimmunoprecipitations of pyrin and caspase-1 from THP-1 human monocytic cells were consistent with the interaction of endogenous proteins. The C-terminal B30.2 domain of pyrin is necessary and sufficient for the interaction, and binding was reduced by FMF-associated B30.2 mutations. Full-length pyrin attenuated IL-1β production in cells transfected with a caspase-1/IL-1β construct, an effect diminished by FMF-associated B30.2 mutations and in B30.2 deletion mutants. Modeling of the crystal structure of caspase-1 with the deduced structure of the pyrin B30.2 domain corroborated both the interaction and the importance of M694V and M680I pyrin mutations. Consistent with a net inhibitory effect of pyrin on IL-1β activation, small interfering RNA (siRNA)-mediated pyrin knockdown in THP-1 cells augmented IL-1β production in response to bacterial LPS. Moreover, the IL-1 receptor antagonist anakinra suppressed acute-phase proteins in a patient with FMF and amyloidosis. Our data support a direct, ASC-independent effect of pyrin on IL-1β activation and suggest heightened IL-1 responsiveness as one factor selecting for pyrin mutations." @default.
• W1974781808 created "2016-06-24" @default.
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• W1974781808 date "2006-06-27" @default.
• W1974781808 modified "2023-10-17" @default.
• W1974781808 title "The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1β production" @default.
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• W1974781808 doi "https://doi.org/10.1073/pnas.0602081103" @default.
• W1974781808 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1479864" @default.
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